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P05042 (FUMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Alternative name(s):
Iron-independent fumarase
Gene names
Name:fumC
Ordered Locus Names:b1611, JW1603
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate. Ref.7

Catalytic activity

(S)-malate = fumarate + H2O. Ref.7

Enzyme regulation

Inhibited by ATP and S-2,3-dicarboxyaziridine. Ref.7

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer. Ref.7 Ref.8 Ref.9 Ref.14 Ref.16

Subcellular location

Cytoplasm HAMAP-Rule MF_00743.

Induction

Under conditions of iron limitation and oxidative stress. Ref.7 Ref.10

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=50 µM for L-malate (at pH 7.3 and 30 degrees Celsius) Ref.7

pH dependence:

Optimum pH is 8.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161275

Regions

Region98 – 1003Substrate binding HAMAP-Rule MF_00743
Region129 – 1324B site HAMAP-Rule MF_00743
Region139 – 1413Substrate binding HAMAP-Rule MF_00743
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1881Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity

Experimental info

Mutagenesis1261R → A: Reduces enzyme activity 10-fold. Ref.12
Mutagenesis1271K → D: No effect. Ref.12
Mutagenesis1291H → N: No effect on activity, but the carboxyamide group from Asn129 swings into the B site and replaces S-malate by forming a bifurcated hydrogen bond with Asn131 and Asp132. Ref.12 Ref.15
Mutagenesis1881H → N: Reduces activity 200-fold. Ref.15
Mutagenesis3151E → Q: Reduces activity 10-fold. Ref.16

Secondary structure

.............................................................. 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05042 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 3D67E3C0F0FDF40B

FASTA46750,489
        10         20         30         40         50         60 
MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE 

        70         80         90        100        110        120 
DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT QSNMNMNEVL ANRASELLGG 

       130        140        150        160        170        180 
VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALRKQL IPQLKTLTQT LNEKSRAFAD 

       190        200        210        220        230        240 
IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EYARRVADEL AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 

       310        320        330        340        350        360 
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG GASGNFELNV 

       370        380        390        400        410        420 
FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ LLNESLMLVT ALNTHIGYDK 

       430        440        450        460 
AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF DSWVRPEQMV GSMKAGR 

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional relationships between fumarase and aspartase. Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of Escherichia coli K12."
Woods S.A., Miles J.S., Roberts R.E., Guest J.R.
Biochem. J. 237:547-557(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Complete nucleotide sequence of the fumarase gene fumA, of Escherichia coli."
Miles J.S., Guest J.R.
Nucleic Acids Res. 12:3631-3642(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
[6]"The fumarase genes of Escherichia coli: location of the fumB gene and discovery of a new gene (fumC)."
Guest J.R., Miles J.S., Roberts R.E., Woods S.A.
J. Gen. Microbiol. 131:2971-2984(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
[7]"Purification and characterization of two types of fumarase from Escherichia coli."
Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.
J. Biochem. 109:728-733(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
[8]"Purification and crystallization of fumarase C from Escherichia coli."
Weaver T.M., Levitt D.G., Banaszak L.J.
J. Mol. Biol. 231:141-144(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, SUBUNIT.
[9]"Two biochemically distinct classes of fumarase in Escherichia coli."
Woods S.A., Shwartzbach S.D., Guest J.R.
Biochim. Biophys. Acta 954:14-26(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOCHEMICAL ANALYSIS OF FUMA AND FUMC, SUBUNIT.
[10]"Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC genes of Escherichia coli: role of the arcA, fnr, and soxR gene products."
Park S.J., Gunsalus R.P.
J. Bacteriol. 177:6255-6262(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[12]"The role of the allosteric B site in the fumarase reaction."
Rose I.A., Weaver T.M.
Proc. Natl. Acad. Sci. U.S.A. 101:3393-3397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-126; LYS-127 AND HIS-129.
[13]"Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci-carboxylate intermediate."
Puthan Veetil V., Fibriansah G., Raj H., Thunnissen A.M., Poelarends G.J.
Biochemistry 51:4237-4243(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTION MECHANISM.
[14]"Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli."
Weaver T., Banaszak L.
Biochemistry 35:13955-13965(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SUBUNIT.
[15]"Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site."
Weaver T., Lees M., Banaszak L.
Protein Sci. 6:834-842(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS ASN-129 AND ASN-188 IN COMPLEX WITH MALATE AND CITRATE, MUTAGENESIS OF HIS-129 AND HIS-188.
[16]"X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation."
Estevez M., Skarda J., Spencer J., Banaszak L., Weaver T.M.
Protein Sci. 11:1552-1557(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT GLN-315, MUTAGENESIS OF GLU-315, SUBUNIT.
[17]"Structure of free fumarase C from Escherichia coli."
Weaver T.
Acta Crystallogr. D 61:1395-1401(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04065 Genomic DNA. Translation: CAA27698.1.
U00096 Genomic DNA. Translation: AAC74683.1.
AP009048 Genomic DNA. Translation: BAA15349.1.
X00522 Genomic DNA. Translation: CAA25205.1.
PIRUFEC. S07138.
RefSeqNP_416128.1. NC_000913.3.
YP_489874.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FUOX-ray1.98A/B1-467[»]
1FUPX-ray2.30A/B1-467[»]
1FUQX-ray2.00A/B1-467[»]
1FURX-ray1.95A/B1-467[»]
1KQ7X-ray2.60A/B1-467[»]
1YFEX-ray2.19A1-467[»]
2FUSX-ray2.20A/B1-467[»]
ProteinModelPortalP05042.
SMRP05042. Positions 4-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9719N.
IntActP05042. 14 interactions.
STRING511145.b1611.

Proteomic databases

PaxDbP05042.
PRIDEP05042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74683; AAC74683; b1611.
BAA15349; BAA15349; BAA15349.
GeneID12934129.
946147.
KEGGecj:Y75_p1587.
eco:b1611.
PATRIC32118524. VBIEscCol129921_1682.

Organism-specific databases

EchoBASEEB0353.
EcoGeneEG10358. fumC.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.
PhylomeDBP05042.

Enzyme and pathway databases

BioCycEcoCyc:FUMC-MONOMER.
ECOL316407:JW1603-MONOMER.
MetaCyc:FUMC-MONOMER.
SABIO-RKP05042.
UniPathwayUPA00223; UER01007.

Gene expression databases

GenevestigatorP05042.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05042.
PROP05042.

Entry information

Entry nameFUMC_ECOLI
AccessionPrimary (citable) accession number: P05042
Secondary accession number(s): P76891
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene